P69447 (ATPH_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit c, chloroplastic

Alternative name(s):
ATP synthase F(0) sector subunit c
ATPase subunit III
F-type ATPase subunit c
Short name=F-ATPase subunit c
Lipid-binding protein

Gene names

Name:

atpH

Encoded on

Plastid; Chloroplast

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. HAMAP MF_01396 Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits. HAMAP MF_01396
Cofactor	The c14 crystal includes 1 chlorophyll and 2 carotenoids.
Subunit structure	F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has four main subunits: a1, b1, b'1 and c(14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Ref.6
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein HAMAP MF_01396.
Miscellaneous	In plastids the F-type ATPase is also known as CF1CF0. HAMAP MF_01396
Sequence similarities	Belongs to the ATPase C chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Chloroplast Membrane Plastid Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding
PTM	Formylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 81

81

ATP synthase subunit c, chloroplastic HAMAP MF_01396

PRO_0000112205

Regions

Transmembrane

3 – 23

21

Helical; Potential

Transmembrane

57 – 77

21

Helical; Potential

Sites

Site

61

1

Reversibly protonated during proton transport By similarity

Amino acid modifications

Modified residue

1

1

N-formylmethionine HAMAP MF_01396

Secondary structure

1

.

.

.

.

.

.

.

81

Helix Strand Turn

Details...

Helix

5 – 12

8

Helix

53 – 65

13

Helix

69 – 75

7

Sequences

	Sequence		Length	Mass (Da)
	P69447 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 75F8DBD4F23A896D	FASTA	81	7,974
	10 20 30 40 50 60 MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM 70 80 EALTIYGLVV ALALLFANPF V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of the proteolipid subunit of the ATP synthase from spinach chloroplasts." Sebald W., Wachter E. FEBS Lett. 122:307-311(1980) Cited for: PROTEIN SEQUENCE.
[2]	"Localization and nucleotide sequence of the gene for the ATP synthase proteolipid subunit on the spinach plastid chromosome." Alt J., Winter P., Sebald W., Moser J.G., Schedel R., Westhoff P., Herrmann R.G. Curr. Genet. 7:129-138(1983) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement." Hennig J., Herrmann R.G. Mol. Gen. Genet. 203:117-128(1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A gene cluster in the spinach and pea chloroplast genomes encoding one CF1 and three CF0 subunits of the H+-ATP synthase complex and the ribosomal protein S2." Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R., Bottomley W. J. Mol. Biol. 196:283-298(1987) [PubMed: 2443718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization." Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R. Plant Mol. Biol. 45:307-315(2001) [PubMed: 11292076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Geant d'hiver and cv. Monatol.
[6]	"Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments." Varco-Merth B., Fromme R., Wang M., Fromme P. Biochim. Biophys. Acta 1777:605-612(2008) [PubMed: 18515064] [Abstract] Cited for: SUBUNIT, PRELIMINARY CRYSTALLIZATION, PIGMENT COMPOSITION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03775 Genomic DNA. Translation: CAA27402.1.
AJ400848 Genomic DNA. Translation: CAB88712.1.

PIR

LWSPA. S14423.

RefSeq

NP_054919.1. NC_002202.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W5J	X-ray	3.80	A/B/C/D/E/F/G/H/I/J/K/L/M/V	2-79	[»]

ProteinModelPortal

P69447.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2715579.

Phylogenomic databases

ProtClustDB

CHL00061.

Family and domain databases

HAMAP

MF_01396. ATP_synth_c_bact.
[Tree]

InterPro

IPR000454. ATPase_F0-cplx_csu.
IPR005953. ATPase_F0-cplx_csu_bac/chlpt.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_F0/V0-cplx_csu.
[Graphical view]

Gene3D

G3DSA:1.20.20.10. ATPase_F0/V0_c. 1 hit.

Pfam

PF00137. ATP-synt_C. 1 hit.
[Graphical view]

PRINTS

PR00124. ATPASEC.

SUPFAM

SSF81333. ATPase_F0/V0_c. 1 hit.

TIGRFAMs

TIGR01260. ATP_synt_c. 1 hit.

PROSITE

PS00605. ATPASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATPH_SPIOL

Accession

Primary (citable) accession number: P69447
Secondary accession number(s): P00843, Q33180, Q9XPT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	September 21, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program